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Q9KDW8 (GLPK_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 68. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycerol kinase

EC=2.7.1.30
Alternative name(s):
ATP:glycerol 3-phosphotransferase
Glycerokinase
Short name=GK
Gene names
Name:glpK
Ordered Locus Names:BH1093
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length497 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Key enzyme in the regulation of glycerol uptake and metabolism. HAMAP MF_00186

Catalytic activity

ATP + glycerol = ADP + sn-glycerol 3-phosphate. HAMAP MF_00186

Pathway

Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1. HAMAP MF_00186

Sequence similarities

Belongs to the FGGY kinase family.

Ontologies

Keywords
   Biological processGlycerol metabolism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processglycerol-3-phosphate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glycerol kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 497497Glycerol kinase HAMAP MF_00186
PRO_0000059433

Regions

Nucleotide binding411 – 4155ATP By similarity

Sites

Binding site131Substrate By similarity
Binding site171ATP By similarity
Binding site831Substrate By similarity
Binding site1351Substrate By similarity
Binding site2451Substrate By similarity
Binding site2671ATP By similarity
Binding site3101ATP; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9KDW8 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 01A822C997243CE1

FASTA49754,856
        10         20         30         40         50         60 
MTKKYILALD QGTTSSRAIL FNEAGEIIGI EQKEFQQIFP KPGWVEHDAN EIWASVLSVI 

        70         80         90        100        110        120 
AGVLLKTNVE AKEIAAIGIT NQRETAVVWE KESGRPIYNA LVWQSRQTAG ICERLRAEGF 

       130        140        150        160        170        180 
SEMVTEKTGL LIDPYFSGTK VRWILDHVDG AQERAERGEL LFGTIDTWLI WKLSGGKAHV 

       190        200        210        220        230        240 
TDYSNASRTL LYNIYEQCWD DELLKMLNVP RAMLPDVRPS SEVYAETVSY HFFGEEIPIA 

       250        260        270        280        290        300 
GAAGDQQAAL FGQACFEKGM AKNTYGTGCF MLMNTGNQGV KSKHGLLTTI AWGLDGKVEY 

       310        320        330        340        350        360 
ALEGSIFVAG SAIQWLRDGL RMMKSAKESE GYATKVTSAD GVYVVPAFVG LGTPYWDSDV 

       370        380        390        400        410        420 
RGAVFGLTRG TSKEHFIRAT LESLAYQTKD VLQAMEADSG ISLKTLRVDG GAVANNFLMQ 

       430        440        450        460        470        480 
FQSDLLGVSV ERPTVQETTA LGAAYLAGLA VGFWTSKEEI TNNWNLEQKF SAEMEETDRA 

       490 
KLYEGWQKAV RAAQAFK 

« Hide

References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed: 11058132] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000004 Genomic DNA. Translation: BAB04812.1.
PIRE83786.
RefSeqNP_241959.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9KDW8.
SMRQ9KDW8. Positions 3-497.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000050050; EBBACP00000048689; EBBACG00000050041.
GeneID892059.
GenomeReviewsGene locus BH1093 in contig BA000004_GR.
KEGGbha:BH1093.
NMPDRfig|272558.1.peg.1093.
PATRIC18939246. VBIBacHal18977_1141.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000001374.
HOGENOMHBG511469.
OMAALYGQLC.
PhylomeDBQ9KDW8.
ProtClustDBPRK00047.

Enzyme and pathway databases

BioCycBHAL272558:BH1093-MONOMER.

Family and domain databases

HAMAPMF_00186. Glycerol_kin.
[Tree]
InterProIPR000577. Carb_kinase_FGGY.
IPR018485. Carb_kinase_FGGY_C.
IPR018483. Carb_kinase_FGGY_CS.
IPR018484. Carb_kinase_FGGY_N.
IPR005999. Glycerol_kin.
[Graphical view]
KOK00864.
PANTHERPTHR10196. FGGY_kin. 1 hit.
PTHR10196:SF9. Glycerol_kin. 1 hit.
PfamPF02782. FGGY_C. 1 hit.
PF00370. FGGY_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01311. Glycerol_kin. 1 hit.
PROSITEPS00933. FGGY_KINASES_1. 1 hit.
PS00445. FGGY_KINASES_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLPK_BACHD
AccessionPrimary (citable) accession number: Q9KDW8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families